Alpha-synuclein fibrillization plays essential role in membrane disruption

H. Chaudhary; V. Subramaniam; M. Claessens

doi:10.1007/s00249-013-0917-x

Abstract

α-synuclein aggregation is involved in the pathogenesis of Parkinson’s disease. The prevailing hypothesis on amyloid toxicity involves membrane disruption by oligomeric species. However, isolated α-synuclein oligomers only transiently disrupt the membrane and vesicles remain intact. We studied synuclein aggregation in giant unilamellar vesicles and observed dramatic membrane disintegration and incorporation of lipids into fibrillar aggregates. Aggregation of α-synuclein in the presence of calcein filled vesicles shows synchronous leakage of dye with fibrillization. The evolving picture suggests that fibrillization and membrane disintegration during the aggregation process may be more relevant for toxicity than permeabilization by stable oligomeric species.

Original language	English
Pages (from-to)	S148-S148
Journal	European biophysics journal
Volume	42
Issue number	Suppl. 1
DOIs	https://doi.org/10.1007/s00249-013-0917-x
Publication status	Published - 2013
Event	9th European Biophysics Congress, EBSA 2013 - Lisbon, Portugal Duration: 13 Jul 2013 → 17 Jul 2013 Conference number: 9

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@article{08b22c412e23437e9beb9273cf5395ef,

title = "Alpha-synuclein fibrillization plays essential role in membrane disruption",

abstract = "α-synuclein aggregation is involved in the pathogenesis of Parkinson{\textquoteright}s disease. The prevailing hypothesis on amyloid toxicity involves membrane disruption by oligomeric species. However, isolated α-synuclein oligomers only transiently disrupt the membrane and vesicles remain intact. We studied synuclein aggregation in giant unilamellar vesicles and observed dramatic membrane disintegration and incorporation of lipids into fibrillar aggregates. Aggregation of α-synuclein in the presence of calcein filled vesicles shows synchronous leakage of dye with fibrillization. The evolving picture suggests that fibrillization and membrane disintegration during the aggregation process may be more relevant for toxicity than permeabilization by stable oligomeric species.",

author = "H. Chaudhary and V. Subramaniam and M. Claessens",

year = "2013",

doi = "10.1007/s00249-013-0917-x",

language = "English",

volume = "42",

pages = "S148--S148",

journal = "European biophysics journal",

issn = "0175-7571",

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number = "Suppl. 1",

note = "9th European Biophysics Congress, EBSA 2013, EBSA ; Conference date: 13-07-2013 Through 17-07-2013",

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TY - JOUR

T1 - Alpha-synuclein fibrillization plays essential role in membrane disruption

AU - Chaudhary, H.

AU - Subramaniam, V.

AU - Claessens, M.

N1 - Conference code: 9

PY - 2013

Y1 - 2013

N2 - α-synuclein aggregation is involved in the pathogenesis of Parkinson’s disease. The prevailing hypothesis on amyloid toxicity involves membrane disruption by oligomeric species. However, isolated α-synuclein oligomers only transiently disrupt the membrane and vesicles remain intact. We studied synuclein aggregation in giant unilamellar vesicles and observed dramatic membrane disintegration and incorporation of lipids into fibrillar aggregates. Aggregation of α-synuclein in the presence of calcein filled vesicles shows synchronous leakage of dye with fibrillization. The evolving picture suggests that fibrillization and membrane disintegration during the aggregation process may be more relevant for toxicity than permeabilization by stable oligomeric species.

AB - α-synuclein aggregation is involved in the pathogenesis of Parkinson’s disease. The prevailing hypothesis on amyloid toxicity involves membrane disruption by oligomeric species. However, isolated α-synuclein oligomers only transiently disrupt the membrane and vesicles remain intact. We studied synuclein aggregation in giant unilamellar vesicles and observed dramatic membrane disintegration and incorporation of lipids into fibrillar aggregates. Aggregation of α-synuclein in the presence of calcein filled vesicles shows synchronous leakage of dye with fibrillization. The evolving picture suggests that fibrillization and membrane disintegration during the aggregation process may be more relevant for toxicity than permeabilization by stable oligomeric species.

U2 - 10.1007/s00249-013-0917-x

DO - 10.1007/s00249-013-0917-x

M3 - Meeting Abstract

SN - 0175-7571

VL - 42

SP - S148-S148

JO - European biophysics journal

JF - European biophysics journal

IS - Suppl. 1

T2 - 9th European Biophysics Congress, EBSA 2013

Y2 - 13 July 2013 through 17 July 2013

ER -

Alpha-synuclein fibrillization plays essential role in membrane disruption

Abstract

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